ArticleBiochimica et biophysica acta2010
Antimicrobial peptides bind more strongly to membrane pores.
Article in Biochimica et biophysica acta, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed.
- Marine Antimicrobial Peptides: From Ocean Biodiversity to Genome Mining, Multi-Omics Discovery, and Biotechnological Innovation in the Battle Against Antimicrobial Resistance.Probiotics and antimicrobial proteins · 2026Review
- Cooperative membrane association as a mechanistic origin of synergistic antimicrobial peptide activity.RSC chemical biology · 2026Review
- Mechanistic Insights into Human Defensin Antimicrobial Activity from Membrane Simulations.The Journal of membrane biology · 2026Article
- Structural and Functional Effects of the Interaction Between an Antimicrobial Peptide and Its Analogs with Model Bacterial and Erythrocyte Membranes.Biomolecules · 2025Article
- Harnessing Non-Antibiotic Strategies to Counter Multidrug-Resistant Clinical Pathogens with Special Reference to Antimicrobial Peptides and Their Coatings.Antibiotics (Basel, Switzerland) · 2025Review
- Investigating How Lysophosphatidylcholine and Lysophosphatidylethanolamine Enhance the Membrane Permeabilization Efficacy of Host Defense Peptide Piscidin 1.The journal of physical chemistry. B · 2025Article
- CHARMM at 45: Enhancements in Accessibility, Functionality, and Speed.The journal of physical chemistry. B · 2024Review
- Investigating Development and Defense Systems in Early Reproductive Stages of Male and Female Gonads in Black ScorpionfishBiology · 2024Article
- How Cell-Penetrating Peptides Behave Differently from Pore-Forming Peptides: Structure and Stability of Induced Transmembrane Pores.Journal of the American Chemical Society · 2023Article
- Peptides Isolated from Amphibian Skin Secretions with Emphasis on Antimicrobial Peptides.Toxins · 2022Review
- Antioxidant and Antimicrobial Peptides Derived from Food Proteins.Molecules (Basel, Switzerland) · 2022Review
- What Makes a Good Pore Former: A Study of Synthetic Melittin Derivatives.Biophysical journal · 2020Article
- Hemoglobin Reassembly of Antimicrobial Fragments from the Midgut ofBiomolecules · 2020Article
- Anti-amoebic activity of a cecropin-melittin hybrid peptide (CM11) against trophozoites of Entamoeba histolytica.Wiener klinische Wochenschrift · 2019Article
- Cystic Fibrosis and Pseudomonas aeruginosa: the Host-Microbe Interface.Clinical microbiology reviews · 2019Review
- Mechanistic Landscape of Membrane-Permeabilizing Peptides.Chemical reviews · 2019Review
- Functional Mechanisms Underlying the Antimicrobial Activity of theInternational journal of molecular sciences · 2019Article
- Computational studies of peptide-induced membrane pore formation.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Computational prediction of the optimal oligomeric state for membrane-inserted β-barrels of protegrin-1 and related mutants.Journal of peptide science : an official publication of the European Peptide Society · 2017Article
- Engineering monolayer poration for rapid exfoliation of microbial membranes.Chemical science · 2017Article
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2 authors.
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Abstract
Antimicrobial peptides (AMPs) are small, usually cationic peptides, which permeabilize bacterial membranes. Understanding their mechanism of action might help design better antibiotics. Using an implicit membrane model, modified to include pores of different shapes, we show that four AMPs (alamethicin, melittin, a magainin analogue, MG-H2, and piscidin 1) bind more strongly to membrane pores, consistent with the idea that they stabilize them. The effective energy of alamethicin in cylindrical pores is similar to that in toroidal pores, whereas the effective energy of the other three peptides is lower in toroidal pores. Only alamethicin intercalates into the membrane core; MG-H2, melittin and piscidin are located exclusively at the hydrophobic/hydrophilic interface. In toroidal pores, the latter three peptides often bind at the edge of the pore, and are in an oblique orientation. The calculated binding energies of the peptides are correlated with their hemolytic activities. We hypothesize that one distinguishing feature of AMPs may be the fact that they are imperfectly amphipathic which allows them to bind more strongly to toroidal pores. An initial test on a melittin-based mutant seems to support this hypothesis.
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